GALNT2

Protein-coding gene in the species Homo sapiens

GALNT2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2FFU, 2FFV, 4D0T, 4D0Z, 4D11, 5AJN, 5AJO, 5AJP, 5FV9

Identifiers

Aliases

GALNT2, GalNAc-T2, polypeptide N-acetylgalactosaminyltransferase 2, CDG2T

External IDs

OMIM: 602274; MGI: 894694; HomoloGene: 3297; GeneCards: GALNT2; OMA:GALNT2 - orthologs

Gene location (Human)

Chr.	Chromosome 1 (human)^[1]

Band	1q42.13	Start	230,057,990 bp^[1]
Band	1q42.13	End	230,282,122 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8\|8 E2	Start	124,958,130 bp^[2]
Band	8\|8 E2	End	125,072,463 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

Descending thoracic aorta

ascending aorta

cartilage tissue

gastric mucosa

right coronary artery

stromal cell of endometrium

body of pancreas

palpebral conjunctiva

right lobe of liver

left coronary artery

Top expressed in

lens

yolk sac

pancreas

stomach

islet of Langerhans

proximal tubule

neural tube

mesencephalon

skeletal muscle tissue

right kidney

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity manganese ion binding glycosyltransferase activity metal ion binding protein binding carbohydrate binding polypeptide N-acetylgalactosaminyltransferase activity
Cellular component	integral component of membrane integral component of Golgi membrane Golgi apparatus membrane Golgi membrane extracellular region Golgi cisterna membrane perinuclear region of cytoplasm Golgi stack extracellular exosome endoplasmic reticulum membrane
Biological process	protein O-linked glycosylation via serine protein glycosylation protein O-linked glycosylation via threonine O-glycan processing protein O-linked glycosylation
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


2590


108148

Ensembl


ENSG00000143641


ENSMUSG00000089704

UniProt


Q10471


Q6PB93

RefSeq (mRNA)


NM_001291866 NM_004481


NM_139272

RefSeq (protein)


NP_001278795 NP_004472


NP_644678

Location (UCSC)

Chr 1: 230.06 – 230.28 Mb

Chr 8: 124.96 – 125.07 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.^[5]^[6]^[7]

This gene encodes polypeptide N-acetylgalactosaminyltransferase 2, a member of the GalNAc-transferases family. This family transfers an N-acetyl galactosamine to the hydroxyl group of a serine or threonine residue in the first step of O-linked oligosaccharide biosynthesis. The localization site of this particular enzyme is preponderantly the trans-Golgi.^[8] Individual GalNAc-transferases have distinct activities, and initiation of O-glycosylation in a cell is regulated by a repertoire of GalNAc-transferases.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143641 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000089704 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Bennett EP, Weghuis DO, Merkx G, van Kessel AG, Eiberg H, Clausen H (Jul 1998). "Genomic organization and chromosomal localization of three members of the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase family". Glycobiology. 8 (6): 547–55. doi:10.1093/glycob/8.6.547. PMID 9592121.
^ White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H (Dec 1995). "Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase". J Biol Chem. 270 (41): 24156–65. doi:10.1074/jbc.270.41.24156. PMID 7592619.
^ ^a ^b "Entrez Gene: GALNT2 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-T2)".
^ Netherton CL, McCrossan MC, Denyer M, Ponnambalam S, Armstrong J, Takamatsu HH, Wileman TE (November 2006). "African Swine Fever Virus Causes Microtubule-Dependent Dispersal of trans-Golgi Network" (PDF). Journal of Virology. 80 (22): 11385–11392. doi:10.1128/JVI.00439-06. PMC 1642160. PMID 16956944.

Bennett EP, Hassan H, Clausen H (1996). "cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3". J. Biol. Chem. 271 (29): 17006–12. doi:10.1074/jbc.271.29.17006. PMID 8663203.
Wandall HH, Hassan H, Mirgorodskaya E, et al. (1997). "Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3". J. Biol. Chem. 272 (38): 23503–14. doi:10.1074/jbc.272.38.23503. PMID 9295285.
Müller S, Goletz S, Packer N, et al. (1997). "Localization of O-glycosylation sites on glycopeptide fragments from lactation-associated MUC1. All putative sites within the tandem repeat are glycosylation targets in vivo". J. Biol. Chem. 272 (40): 24780–93. doi:10.1074/jbc.272.40.24780. PMID 9312074.
Röttger S, White J, Wandall HH, et al. (1998). "Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus". J. Cell Sci. 111 (1): 45–60. doi:10.1242/jcs.111.1.45. PMID 9394011.
Mattu TS, Pleass RJ, Willis AC, et al. (1998). "The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fc alpha receptor interactions". J. Biol. Chem. 273 (4): 2260–72. doi:10.1074/jbc.273.4.2260. PMID 9442070.
Iwasaki H, Zhang Y, Tachibana K, et al. (2003). "Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2". J. Biol. Chem. 278 (8): 5613–21. doi:10.1074/jbc.M211097200. PMID 12438318.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Marcos NT, Cruz A, Silva F, et al. (2003). "Polypeptide GalNAc-transferases, ST6GalNAc-transferase I, and ST3Gal-transferase I expression in gastric carcinoma cell lines". J. Histochem. Cytochem. 51 (6): 761–71. doi:10.1177/002215540305100607. PMID 12754287. S2CID 16133163.
Kinarsky L, Suryanarayanan G, Prakash O, et al. (2004). "Conformational studies on the MUC1 tandem repeat glycopeptides: implication for the enzymatic O-glycosylation of the mucin protein core". Glycobiology. 13 (12): 929–39. doi:10.1093/glycob/cwg109. PMID 12925576.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.